Solid-state NMR spectroscopy will continue to be developed and applied to the study of peptides. Solid-state NMR studies of crystalline peptides and of peptides complexed with lipids and proteins offer favorable opportunities for both the development of spectroscopic methods and the application of these methods to important biological problems. Many biological properties are expressed by peptides, however the primary high resolution methods of structure determination, x-ray diffraction and multidimensional solution NMR spectroscopy, have considerable difficulty in dealing with peptides because they are difficult to crystallize and because of their conformational flexibility. The planned spectroscopic developments involve a wide variety of multidimensional solid-state NMR experiments on polycrystalline and single crystal samples of peptides. The applications are to 20 - 25 residue amphipathic and hydrophobic peptides in lipid bilayers and to several peptides bound to proteins.